抄録
In the yeast, Rhodosporidium toruloides, the mating reaction between two haploid cells designated as A and a type is controlled by pheromone-like substances secreted from each mating type cell. At the initial step of mating reaction, A type cells secrete a factor named rhodotorucine A which induces mating tube formation in the opposite a type cells. In this paper, we presented the isolation and structural elucidation of rhodotorucine A which contains a novel lipophilic amino acid, S-farnesyl cystein, at the C-terminus. The amino acid sequence of rhodotorucine A was determined by dansyl-Edman degradation and enzymatic hydrolyses. Presence of S-farnesyl cystein at the C-terminus of rhodotorucine A was disclosed by proton magnetic resonance, mass spectrometry and chemical synthesis. We proposed the following structure for rhodotorucine A. H-Tyr-Pro-Glu-Ile-Ser-Trp-Thr-Arg-Asn-Gly-Cys(S-farnesyl)-OH
